GenomeNet

Database: UniProt
Entry: P17765
LinkDB: P17765
Original site: P17765 
ID   POLG_BYMV               Reviewed;        3056 AA.
AC   P17765; Q65887; Q6Y1D8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   18-SEP-2019, entry version 130.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-a;
DE              Short=NIa;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Bean yellow mosaic virus.
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12197;
OH   NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH   NCBI_TaxID=4627; Canna.
OH   NCBI_TaxID=3828; Crotalaria.
OH   NCBI_TaxID=52517; Eustoma.
OH   NCBI_TaxID=58987; Freesia.
OH   NCBI_TaxID=49747; Gladiolus.
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=3873; Lupinus luteus (European yellow lupine).
OH   NCBI_TaxID=3879; Medicago sativa (Alfalfa).
OH   NCBI_TaxID=3469; Papaver somniferum (Opium poppy).
OH   NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH   NCBI_TaxID=35938; Robinia pseudoacacia (Black locust).
OH   NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH   NCBI_TaxID=57577; Trifolium pratense (Red clover).
OH   NCBI_TaxID=3899; Trifolium repens (Creeping white clover).
OH   NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH   NCBI_TaxID=97047; Trifolium vesiculosum.
OH   NCBI_TaxID=78534; Trigonella foenum-graecum (Fenugreek).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH   NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate GDD;
RX   PubMed=14648299; DOI=10.1007/s00705-003-0185-7;
RA   Hammond J., Hammond R.W.;
RT   "The complete nucleotide sequence of isolate BYMV-GDD of Bean yellow
RT   mosaic virus, and comparison to other potyviruses.";
RL   Arch. Virol. 148:2461-2470(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2775-3056.
RX   PubMed=2671258; DOI=10.1099/0022-1317-70-8-1961;
RA   Hammond J., Hammond R.W.;
RT   "Molecular cloning, sequencing and expression in Escherichia coli of
RT   the bean yellow mosaic virus Capsid protein gene.";
RL   J. Gen. Virol. 70:1961-1974(1989).
RN   [3]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in
CC       the regulation of viral RNA amplification.
CC   -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: Helper component proteinase: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a
CC       Gly-Gly dipeptide at its own C-terminus. Interacts with virions
CC       and aphid stylets. Acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing
CC       (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May have RNA-binding activity (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
CC       may be involved in replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus
CC       replication. {ECO:0000250}.
CC   -!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that
CC         vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
CC         Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
CC         natural substrate is the viral polyprotein, but other proteins
CC         and oligopeptides containing the appropriate consensus sequence
CC         are also cleaved.; EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus,
CC         commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
CC         processing of the potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P17765-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ95-1; Sequence=External;
CC         Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved
CC       in interaction with stylets. The central part is involved in
CC       interaction with virions and the C-terminus is involved in cell-to
CC       cell movement of the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       attached to the 5'-end of the genomic RNA. This uridylylated form
CC       acts as a nucleotide-peptide primer for the polymerase (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo
CC       post-translational proteolytic processing. Genome polyprotein is
CC       processed by NIa-pro, P1 and HC-pro proteinases resulting in the
CC       production of at least ten individual proteins. P3N-PIPO
CC       polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC       the production of three individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini
CC       autocatalytically. 6K1 is essential for proper proteolytic
CC       separation of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; AY192568; AAP30002.1; -; Genomic_RNA.
DR   EMBL; D00490; BAA00378.1; -; Genomic_RNA.
DR   PIR; JU0115; JU0115.
DR   MEROPS; C04.008; -.
DR   PRIDE; P17765; -.
DR   Proteomes; UP000007620; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Helical capsid protein; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW   Serine protease; Suppressor of RNA silencing; Thiol protease;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN         1   3056       Genome polyprotein.
FT                                /FTId=PRO_0000419996.
FT   CHAIN         1    284       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040256.
FT   CHAIN       285    741       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040257.
FT   CHAIN       742   1089       Protein P3. {ECO:0000255}.
FT                                /FTId=PRO_0000040258.
FT   CHAIN      1090   1142       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040259.
FT   CHAIN      1143   1777       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040260.
FT   CHAIN      1778   1830       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040261.
FT   CHAIN      1831   2021       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040262.
FT   CHAIN      2022   2264       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040263.
FT   CHAIN      2265   2783       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040264.
FT   CHAIN      2784   3056       Capsid protein. {ECO:0000250}.
FT                                /FTId=PRO_0000040265.
FT   DOMAIN      139    284       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      619    741       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1214   1366       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1385   1544       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2022   2240       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2507   2630       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1227   1234       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       335    338       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       593    595       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1316   1319       DECH box.
FT   MOTIF      1871   1878       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    192    192       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    201    201       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    232    232       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    627    627       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    700    700       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2067   2067       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2102   2102       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2172   2172       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        284    285       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        741    742       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1100   1101       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1152   1153       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1787   1788       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1840   1841       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2021   2022       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2274   2275       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2793   2794       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1893   1893       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
FT   VARIANT    2775   2775       D -> G.
FT   VARIANT    2805   2805       D -> N.
FT   VARIANT    2855   2855       L -> F.
FT   VARIANT    2862   2862       E -> K.
FT   VARIANT    2897   2897       Q -> R.
FT   VARIANT    2975   2975       G -> E.
FT   VARIANT    2994   2994       K -> E.
FT   VARIANT    3017   3017       G -> A.
SQ   SEQUENCE   3056 AA;  347722 MW;  BA4D2F2D2D4624B3 CRC64;
     MTTINIGTIP VVINQNADTQ MGEGTKNIFP IVKDFVDPFA DLEMRCAERV KRMGELCFSK
     KGRYITMIPK PDYIKAREKE QREEELNFQN SEHVLNSLDT TCTPEHHSSR NNGMQVSFKT
     QHYKRTFRKP RIQAKKRDLK GQHTIHYVAK ELLSIVKKRD MVLEVVDKRK HANFATFRRY
     GKTYGMHITL NHMVRKRRRV DVTLNKLMTE IAMHCAIPFE CLNTLTLRKG HSGLVLQTET
     VPNVHKIKSK ITIVRGVVNE GNIPVLIDAR KKLSGRDMST IREFSAGDLF WKGYNQTFID
     NRPTDLNHQC TSDLNVTQCG SVMALLTLAL FPCGRITCKK CVENFLNQNN KERFNNASVF
     INQVIQLLEK GFSEFKHSKE ILLMFKERLQ MENPATDQCM EIAKATAALP EAPFSHIKEI
     NNVLLKYGSL SNEEVGGASK HLLEVVRYIR NRTDSIQRND LSKFRNKISS KTHINLDLMC
     DNQLDKNANF VWGQRAYHAK RFLSNYFNEI NPSEGYDKFI FRKLPNGARE LAIGRLIMPT
     NFEAFREQMK GKMIDNGPIG KDCVSRMRGS FCYPCCCTTD DVGTAVISDF KMPTKYHLVL
     GGNDLAKYIK LPTDTTGNMY IAKDGFCHIN IFFAMLVNVS EEKSKDFTKM VRDQIMPKLG
     EWPTMMDVAT ACWQLTVWFP DTLSAELPRI LVDHKLGIMH VLDSYGSISA GYHVLKANIV
     SQLIKFASDD LESELKYYRV GGDCNFGSRV RIDTKFLLKS IYRPDLLERI IEHEPFVLVL
     AMQSPAVLLA LFNSASLEKA VQYWMHREMQ VSHIMTLLAV LASNVSASKL LTTQFEIIEA
     SAPQILAEMD KVHLPMHSIH SANVFLMNMS ESRETDKTID ELGFYSFKKS SRILMEKTLM
     ADLEEQWQGL GLLERLSLIK RSWRVRAKYS SFAIQREEPG IRDKFTTSLK LSGAQIKQQL
     LAQKDQAVHF VERRIEGTKK FVANQSISLI KMCLPRLADI VNILTVIALL NAILAFMLDH
     IKRFNEARRI AQEKKEKQHL KELNTLYNKY WDNEKPTYLE FKSDVIEKLP HTLATFEKYY
     FEDDKYTFQA KPNDMVALEK IIAVTALVLM IFDAERSDCV YKVLNKLKGI LSTTTQDAYR
     FQSLDTSKTL LEEKEMTIDF EINEGEVKAF SGTQTTFSEW WDNQLQNGNV ITHYRTEGQF
     MEFTRANAQP VANEIAHNDA HDILVRGAVG SGKSTGLPFY LSNKGKVLMI ESTRPLAENV
     FKQLKSEPFY ASPTLRMRGT TSYGASPITI MTSGYALHYY ANNPAMMKEY KFVIIDECHV
     HDANAIAFVS LLKEYSFDGK LIKVSATPPG REVEFTTQYP VTLVTEESLS FEQFVSQQGT
     GANCDMLDVC DNILVYVASY NEVDQLSKML LDRGHIVTKV DGRTMKNGKT EIESKGSRSK
     RHFIVATNII ENGVTLDIEG VVDFGLKVVP ELDVDNRLMR YTKQNVSYGE RIQRLGRVGR
     HKAGKALRIG VTEKGLVKPP SVITTEAAFY CFAYGLPVMA EGVTPSLLSK CTVQQARSMM
     SFELPIMYTV NLVRFDGTMH PSVHNLLKPY KLRDSNVVLN KMAIPHGNVR NWPTVRDFKC
     MGVRIDAPED TRVPFHARDI PDKLHKEIFE VCCKYKGDAG FSKLNVVNAC KIAYTLQTDP
     SSIQRTIKIL DELIAREQQK REYFQNVANT SCAGSSYSLS NIINAIRARS TSDYTQENLS
     VLHSARAQLL EFKNINSDFS NLSTLSEFGA LECLQFESLQ EISKHLQLKG HWNKPVLIQD
     FLIAAGVLGG GCWMLYQYFK QETSKAFVFQ GKNRRTKQKL RFRDARDMKG RMEVYADEGT
     IVENFGSKYT KKGKVRGTTT GMGTKTRRFT NMYGFDPTEY SFARYLDPIT GETLDEQPIT
     NLNLVSEHFQ EMRRKYRENE IMESQQFAAN PRIEAYFVKD AGQKVLKVDL TPHKPLLYSD
     KFGNIMGYPE REGELRQTGA AEFIDPKELP EPKESTDFDF ESLSKIGGLR DYNPIAANVC
     LLENESAEYC DEIYGIGYGN VIITNQHLFR HNNGELTIKS KHGTFKCKNT CALKLLPIEG
     HDLLLIQMPK DFPVFPQKLR FREPTHEDKI VLVSTNFQEK SFSSVVSESS NISRVKQANF
     FKHWISTVAG QCGNPMVSTK DGFIVGIHSL TAVSGDLNVF TSIPPNFEDE VLKQMSKKSW
     CCGWKLNMSQ IGWDGIKIVD DQPKDPFPVS KMVGLLNDLQ LSFQSAKNTK WLLERAHGNI
     KAVAQASSAL VTKHVVKGKC RLFEVYLTTD EEAEKFFRPL MGAYQKSRLN KEAYVKDLMK
     YATPIEVGLV DTRCFERSFE KVQNMLELKG FSKCNYVTYG PDILSALNMK AAMGALYSGK
     KKDHFSEISE EKFDNILQAS CERLYSGRMG VWNGSLKAEL RPQEKVLANK TRSFTAAPID
     TLLAGKVCVD DFNNKFYSLH LKIPSTVGIT KFYGGWDRLL DSLPDGWVYC DADGSQFDSS
     LTPYLLNAVL EMRLRLMEEW DLGEQMLKNL YTEIVYTPIL TPDGTIVKKF KGNNSGQPST
     VVDNTLMVIM AVYYAAEKLG IKGNLEDTLV FFANGDDLLI AIKPECESYL DKFEGLFSEL
     GLKYDFSSRT KNKGDLWFMS HRGIQIDGMW IPKLEEERIV SILEWDRAIQ PEHRLEAICA
     AMIEAWGYPT LLNHIRKFYL WVLGQAPYSQ LSAEGKAPYI SEVALKHLYT EEKVTPTELE
     RYNIALIDCF ESESDEVLTC RFQSDQEQLN AGEEKKDKRK KNEGDPNKDS EGQSVRQIVP
     DRDVNAGTVG TFSVPRLKKI AGKLNIPKIG GKIVLNLDHL LEYNPPQDDI SNVIATQAQF
     EAWYNGVKQA YEVEDSQMGI ILNGLMVWCI ENGTSGDLQG EWTMMDGEEQ VTYPLKPILD
     NAKPTFRQIM SHFSEVAEAY IEKRNATERY MPRYGLQRNL TDYGLARYAF DFYKLTSRTP
     VRAREAHMQM KAAAVRGKST RLFGLDGNVG TDEENTERHT AGDVNRDMHT MLGVRI
//
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